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Entry: B7CB08_9FIRM
LinkDB: B7CB08_9FIRM
Original site: B7CB08_9FIRM 
ID   B7CB08_9FIRM            Unreviewed;       876 AA.
AC   B7CB08;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138, ECO:0000256|PIRNR:PIRNR000853};
DE            EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
GN   Name=ppdK {ECO:0000313|EMBL:EEC90072.1};
GN   ORFNames=EUBIFOR_01379 {ECO:0000313|EMBL:EEC90072.1};
OS   Holdemanella biformis DSM 3989.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemanella.
OX   NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC90072.1, ECO:0000313|Proteomes:UP000004315};
RN   [1] {ECO:0000313|EMBL:EEC90072.1, ECO:0000313|Proteomes:UP000004315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC90072.1,
RC   ECO:0000313|Proteomes:UP000004315};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEC90072.1, ECO:0000313|Proteomes:UP000004315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC90072.1,
RC   ECO:0000313|Proteomes:UP000004315};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Eubacterium biforme (DSM 3989).";
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000853};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3};
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEC90072.1}.
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DR   EMBL; ABYT01000074; EEC90072.1; -; Genomic_DNA.
DR   RefSeq; WP_003865171.1; NZ_DS996842.1.
DR   AlphaFoldDB; B7CB08; -.
DR   STRING; 518637.EUBIFOR_01379; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   HOGENOM; CLU_015345_0_2_9; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000004315; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.80.30; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 2.
DR   PIRSF; PIRSF000853; PPDK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:EEC90072.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000853-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000853-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000313|EMBL:EEC90072.1};
KW   Transferase {ECO:0000313|EMBL:EEC90072.1}.
FT   DOMAIN          58..292
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          306..356
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          422..503
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          519..870
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        455
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   ACT_SITE        832
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   BINDING         561
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         617
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         746
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         746
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         767
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         768
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         769
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         770
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         770
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ   SEQUENCE   876 AA;  97741 MW;  E4C936CD05256E66 CRC64;
     MDKKYVYEFN EGDETMRELL GGKGANLAGM SKLGMPVPYG FTITTEACNQ YYEDNETIND
     GIKTQIMEYL DLLEKKSGKK LGDEANPLLV SVRSGARASM PGMMDTILNL GMNKTVAETV
     ANLTNNERFA YDSYRRFIQM YSDVVMGLSK KRFEEIIDEV KAERGITDDL DLNAEDMKKL
     VELFKAFYKN ELKSEFPEEP KEQLMGAIEA VFRSWNNPRA IYYRKMNDIP SSWGTAVNVQ
     MMVFGNMGND CGTGVAFTRN PSTGENKLYG EFLMNAQGED VVAGIRTPQK IDQLKEVAPG
     AYDDFVAITK KLETHYRNMQ DMEFTIEKGK LFMLQTRNGK RTAQAALKIA CDMVDEGMIT
     TDEALMMVEP KQLDSLLHPM FDADELKKAE PIATALPASP GAACGQIVFS AEEAIQEASR
     NHKVILVRLE TSPEDIEGMH VSQGILTVRG GMTSHAAVVA RGMGACCVSG CGDINMHDDE
     GYFEIDGVKY HRGDWISLDG STGNIYGSAI KTVPASISGD FERFMNWADE RRTLKVRTNA
     DTPHDAKQAH EFGAQGIGLV RTEHMFFEGD RIKAVREMIV SKTAAQRRVA LEKILPMQRS
     DFEGIYEAMQ GLPVTIRYLD PPLHEFLPTN SYDITQLAKD MHIGLDELKS VISSLHEFNP
     MMGHRGCRLA ISYPEIAEMQ TTAVIQAALA VNERHPDWKI EPEIMIPLVG DVAELRYVKK
     VVCDVADKLI QESEFDMKYH VGTMIEIPRA ALLADEIAKE AEFFSFGTND LTQMTFGFSR
     DDAGGFLQDY YDKKIFEQDP FAHLDQRGVG KLVKMATELG RSTHPNIKLG ICGEHGGDPA
     SIEFCHRVGL NYVSCSPYRV PIARLAAAQA AIKFDK
//
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